ID F4W539_ACREC Unreviewed; 701 AA.
AC F4W539;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Semaphorin-1A {ECO:0000313|EMBL:EGI70735.1};
GN ORFNames=G5I_00530 {ECO:0000313|EMBL:EGI70735.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI70735.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00352}.
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DR EMBL; GL887596; EGI70735.1; -; Genomic_DNA.
DR AlphaFoldDB; F4W539; -.
DR STRING; 103372.F4W539; -.
DR eggNOG; KOG3611; Eukaryota.
DR InParanoid; F4W539; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030215; F:semaphorin receptor binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR CDD; cd11237; Sema_1A; 1.
DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR042068; SEM1A_sema_dom.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR027231; Semaphorin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR11036; SEMAPHORIN; 1.
DR PANTHER; PTHR11036:SF127; SEMAPHORIN-1A; 1.
DR Pfam; PF01437; PSI; 1.
DR Pfam; PF01403; Sema; 1.
DR SMART; SM00423; PSI; 1.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF103575; Plexin repeat; 1.
DR SUPFAM; SSF101912; Sema domain; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 4: Predicted;
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 558..580
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..432
FT /note="Sema"
FT /evidence="ECO:0000259|PROSITE:PS51004"
FT REGION 632..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 701 AA; 77440 MW; 7165BBF1CCAEFB05 CRC64;
MVGGRNLVHN LSLTDLTEQQ RLTWYSTEND VKMCVVKGTP EENCQNYIRI LVKTGPNNLF
VCATNAFKPM CRDYTVHAGN YTIVKEKGGQ ARCPYDPQHN STFVYVDGEL YTGTVADFAG
MDPIIYREPL QTEQYDSMSL NAPNFVSSMS QGDFVYFFFR ETAVEYINCG KAVYSRVARV
CKYDRGGPHR FRNRWTSFLK SRLNCSVTGD FPFYFNEIQS TTELISGQYG GTSAQLIYGT
FTTPVNSISG SAVCAFSLQD IADTFAGNFK EQSAMNSNWL PVQDTKVPDP RPGQCTNDSR
TLPDLTLNFI NTHSLMDESV PSFFGQPIVI RTSFHYRFTQ IAVDPQVKTP GGKTYDVLFI
GTDNGKVIKA VNAESADSHQ KVSPVVIEEI QAFPPTVPVR GIKVVRASQA GDGLEDGRLV
VIADSQVQAL RLHRCYSDRI LSCSECVALQ DPYCAWDKVE NKCRALVGPA ATDASRFLQS
VATGMHASCP ASKSLNKDAG SVGAISANQN KFPQDSIPNK DSPGGEIINI MQDEEQDNSG
PEVSAADTPP PQYSVETLVM AVVAGALAAL FVGFVAGYLC GRKCRKDEDD NLPYPDTEYE
YFEQRQNVNR LAPEPKLLPQ EEVTYAEPVL VPQPPKLQSP KGTMRKPPPT PTETLFQFPD
GYGFRGGPRG DNFGTLRSHQ GDAYRRNDGF ATTRSVKKVY L
//